Design and Implementation of Two-Dimensional Polymer Adsorption Models: Evaluating the Stability of Candida antarctica Lipase B/Solid-Support Interfaces by QCM-D

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• 作者：Sara V. Orski ; Santanu Kundu ; Richard Gross ; Kathryn L. Beers
• 刊名：Biomacromolecules
• 出版年：2013
• 出版时间：February 11, 2013
• 年：2013
• 卷：14
• 期：2
• 页码：377-386
• 全文大小：525K
• 年卷期：v.14,no.2(February 11, 2013)
• ISSN：1526-4602

文摘

A two-dimensional model of a solid-supported enzyme catalyst bead is fabricated on a quartz crystal microbalance with dissipation monitoring (QCM-D) sensor to measure in situ interfacial stability and mechanical properties of Candida antarctica Lipase B (CAL B) under varied conditions relating to ring-opening polymerization. The model was fabricated using a dual photochemical approach, where poly(methyl methacrylate) (PMMA) thin films were cross-linked by a photoactive benzophenone monolayer and blended cross-linking agent. This process produces two-dimensional, homogeneous, rigid PMMA layers, which mimic commercial acrylic resins in a QCM-D experiment. Adsorption of CAL B to PMMA in QCM-D under varied buffer ionic strengths produces a viscoelastic enzyme surface that becomes more rigid as ionic strength increases. The rigid CAL B/PMMA interface demonstrates up to 20% desorption of enzyme with increasing trace water content. Increased polycaprolactone (PCL) binding at the enzyme surface was also observed, indicating greater PCL affinity for a more hydrated enzyme surface. The enzyme layer destabilized with increasing temperature, yielding near complete reversible catalyst desorption in the model.